De Lorenzo, Molea: Riattivazione enzimatica del pepsinogeno ridotto

De Lorenzo, Francesco and Molea, Guido:
Riattivazione enzimatica del pepsinogeno ridotto
Atti della Accademia Nazionale dei Lincei. Classe di Scienze Fisiche, Matematiche e Naturali. Rendiconti Serie 8 42 (1967), fasc. n.1, p. 65-68, (Italian)
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Sunto

An enzyme purified from beef liver microsomes has been shown to catalyze sulfhydryl-disulfide interchange in proteins containing unnatural disulfide bonds, deliberately introduced in the molecules. As previously described fully reduced and randomly crosslinked bovine pancreatic ribonucléase, egg white lysozime and soy bean trypsin inhibitor can be used as substrates for the disulfide interchange enzyme. The present experiments deal with the enzymic reactivation of fully reduced pepsinogen. The purified microsomal disulfide interchange enzyme catalyzes 45% and 75% reactivation of fully reduced pepsinogen respectively in 10 and 20 minutes, in the presence of 5 X 10^-4M dehydroascorbic acid. These results give further strong evidence for the generalized function of the enzyme.

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Referenze Bibliografiche